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- PDB-1cfe: P14A, NMR, 20 STRUCTURES -

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Basic information

Entry
Database: PDB / ID: 1cfe
TitleP14A, NMR, 20 STRUCTURES
ComponentsPATHOGENESIS-RELATED PROTEIN P14A
KeywordsPATHOGENESIS-RELATED PROTEIN / PR-1 PROTEINS / PLANT DEFENSE
Function / homology
Function and homology information


sexual reproduction / defense response to fungus / killing of cells of another organism / extracellular space
Similarity search - Function
CRISP family signature 2. / Allergen V5/Tpx-1-related, conserved site / CRISP family signature 1. / Cysteine-rich secretory protein-related / Pathogenesis-related Protein p14a / CAP / SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains. / CAP domain / Cysteine-rich secretory protein family / CAP superfamily ...CRISP family signature 2. / Allergen V5/Tpx-1-related, conserved site / CRISP family signature 1. / Cysteine-rich secretory protein-related / Pathogenesis-related Protein p14a / CAP / SCP / Tpx-1 / Ag5 / PR-1 / Sc7 family of extracellular domains. / CAP domain / Cysteine-rich secretory protein family / CAP superfamily / 3-Layer(aba) Sandwich / Alpha Beta
Similarity search - Domain/homology
Pathogenesis-related leaf protein 6
Similarity search - Component
Biological speciesSolanum lycopersicum (tomato)
MethodSOLUTION NMR / distance geometry
AuthorsFernandez, C. / Szyperski, T. / Bruyere, T. / Ramage, P. / Mosinger, E. / Wuthrich, K.
Citation
Journal: J.Mol.Biol. / Year: 1997
Title: NMR solution structure of the pathogenesis-related protein P14a.
Authors: Fernandez, C. / Szyperski, T. / Bruyere, T. / Ramage, P. / Mosinger, E. / Wuthrich, K.
#1: Journal: Plant Physiol. / Year: 1995
Title: Pathogenesis-Related Pr-1 Proteins are Antifungal. Isolation and Characterization of Three 14-Kilodalton Proteins of Tomato and of a Basic Pr-1 of Tobacco with Inhibitory Activity Against Phytophthora Infestans
Authors: Niderman, T. / Genetet, I. / Bruyere, T. / Gees, R. / Stintzi, A. / Legrand, M. / Fritig, B. / Mosinger, E.
#2: Journal: Embo J. / Year: 1985
Title: Amino Acid Sequence of the Pathogenesis-Related Leaf Protein P14 from Viroid-Infected Tomato Reveals a New Type of Structurally Unfamiliar Proteins
Authors: Lucas, J. / Camacho Henriquez, A. / Lottspeich, F. / Henschen, A. / Sanger, H.L.
History
DepositionNov 8, 1996Processing site: BNL
Revision 1.0Nov 12, 1997Provider: repository / Type: Initial release
Revision 1.1Mar 24, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Feb 16, 2022Group: Database references / Derived calculations / Other
Category: database_2 / pdbx_database_status ...database_2 / pdbx_database_status / pdbx_struct_assembly / pdbx_struct_oper_list
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_database_status.process_site
Revision 1.4Nov 13, 2024Group: Data collection / Structure summary
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / pdbx_entry_details / pdbx_modification_feature

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: PATHOGENESIS-RELATED PROTEIN P14A


Theoretical massNumber of molelcules
Total (without water)14,9141
Polymers14,9141
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
Representative

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Components

#1: Protein PATHOGENESIS-RELATED PROTEIN P14A / PATHOGENESIS-RELATED LEAF PROTEIN 6 / ETHYLENE INDUCED PROTEIN P1 / P14


Mass: 14914.463 Da / Num. of mol.: 1 / Fragment: RESIDUES 1 - 135
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Solanum lycopersicum (tomato) / Organ: LEAF / Production host: Escherichia coli (E. coli) / References: UniProt: P04284
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experimentType: SEE PAPER *JRNL*

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Sample preparation

Sample conditionspH: 5.5 / Temperature: 303 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker AMXBrukerAMX6001
Varian UNITYPLUSVarianUNITYPLUS7502

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Processing

NMR software
NameDeveloperClassification
OPALWUTHRICHrefinement
DIANAstructure solution
RefinementMethod: distance geometry / Software ordinal: 1
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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